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Resonance Raman spectroscopy of sensory rhodopsin II from Natronobacterium pharaonis
Author(s) -
Gellini Cristina,
Lüttenberg Beate,
Sydor Jens,
Engelhard Martin,
Hildebrandt Peter
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01472-1
Subject(s) - protonation , raman spectroscopy , chemistry , resonance raman spectroscopy , schiff base , resonance (particle physics) , rhodopsin , absorption spectroscopy , spectroscopy , hydrogen bond , spectral line , crystallography , stereochemistry , photochemistry , molecule , biochemistry , atomic physics , organic chemistry , optics , retinal , physics , ion , quantum mechanics , astronomy
Sensory rhodopsin II (pSRII), the photophobic receptor from Natronobacterium pharaonis , has been studied by time‐resolved resonance Raman (RR) spectroscopy using the rotating cell technique. Upon excitation with low laser power, the RR spectra largely reflect the parent state pSRII 500 whereas an increase of the laser power leads to a substantial accumulation of long‐lived intermediates contributing to the RR spectra. All RR spectra could consistently be analysed in terms of four component spectra which were assigned to the parent state pSRII 500 and the long‐lived intermediates M 400 , N 485 and O 535 based on the correlation between the C=C stretching frequency and the absorption maximum. The parent state and the intermediates N 485 and O 535 exhibit a protonated Schiff base. The C=N stretching frequencies and the H/D isotopic shifts indicate strong hydrogen bonding interactions of the Schiff base in pSRII 500 and O 535 whereas these interactions are most likely very weak in N 485 .